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Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K

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Abstract

Both microcalorimetric determination of displacement adsorption enthalpies ΔH and measurement of adsorbed amounts of guanidine – denatured lysozyme (Lys) refolding on the surface of hydrophobic interaction chromatography (HIC) packings at 308 K were carried out and compared with that at 298 K. Study shows that both temperature and concentration of guanidine hydrochloride (GuHCl) affect the molecular mechanism of hydrophobic interaction of protein with adsorbent based on the analysis of dividing ΔH values into three kinds of enthalpy fractions. The adsorption in higher concentrations of GuHCl (>1.3 mol L–1) at 308 K is an enthalpy-driving process, and the adsorption under other GuHCl concentrations is an entropy-driving process. The fact that the Lys denatured by 1.8 mol L–1 GuHCl forms a relatively stable intermediate state under the studied conditions will not be changed by temperature.

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Authors and Affiliations

  1. College of Environment and Chemical Engineering, Xi’an Politechnic University, Xi’an, China, 710048

    Geng X. P., Wu Y. N. & Zhang H. F.

  2. College of Textile Engineering and Material, Xi’an Politechnic University, Xi’an, China, 710048

    Xing J. W.

  3. Institute of Physical Chemistry, Peaking University, Beijing, China, 100871

    Wang B. H.

  4. Institute of Modern Separation Science, Northwest University, Xi’an, China, 710069

    Geng X. D.

Authors
  1. Geng X. P.
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  2. Wu Y. N.
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  3. Wang B. H.
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  4. Zhang H. F.
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  5. Geng X. D.
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  6. Xing J. W.
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Correspondence to Geng X. P..

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Geng, X.P., Wu, Y.N., Wang, B.H. et al. Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K. J Therm Anal Calorim 85, 601–608 (2006). https://doi.org/10.1007/s10973-006-7645-8

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  • DOI: https://doi.org/10.1007/s10973-006-7645-8

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